MPPA1_ARATH
ID MPPA1_ARATH Reviewed; 503 AA.
AC Q9ZU25; Q0WW81; Q8L9K3;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial;
DE AltName: Full=Alpha-MPP 1;
DE AltName: Full=Complex III subunit II;
DE AltName: Full=Core protein II;
DE AltName: Full=Cytochrome b-c1 complex subunit 2-1, mitochondrial;
DE AltName: Full=Inactive zinc metalloprotease alpha-1 {ECO:0000305};
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase core protein 2-1;
DE Flags: Precursor;
GN Name=MPPalpha1;
GN OrderedLocusNames=At1g51980 {ECO:0000312|Araport:AT1G51980};
GN ORFNames=F5F19.4 {ECO:0000312|EMBL:AAD12673.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBUNIT.
RX PubMed=12970493; DOI=10.1104/pp.103.024620;
RA Eubel H., Jansch L., Braun H.P.;
RT "New insights into the respiratory chain of plant mitochondria.
RT Supercomplexes and a unique composition of complex II.";
RL Plant Physiol. 133:274-286(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18189341; DOI=10.1021/pr700595p;
RA Meyer E.H., Taylor N.L., Millar A.H.;
RT "Resolving and identifying protein components of plant mitochondrial
RT respiratory complexes using three dimensions of gel electrophoresis.";
RL J. Proteome Res. 7:786-794(2008).
RN [9]
RP SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=18305213; DOI=10.1104/pp.107.111260;
RA Zsigmond L., Rigo G., Szarka A., Szekely G., Oetvoes K., Darula Z.,
RA Medzihradszky K.F., Koncz C., Koncz Z., Szabados L.;
RT "Arabidopsis PPR40 connects abiotic stress responses to mitochondrial
RT electron transport.";
RL Plant Physiol. 146:1721-1737(2008).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000250|UniProtKB:P11914}.
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c. {ECO:0000250|UniProtKB:P07257}.
CC -!- SUBUNIT: Heterodimer of alpha and beta subunits, forming the
CC mitochondrial processing protease (MPP) in which subunit alpha is
CC involved in substrate recognition and binding and subunit beta is the
CC catalytic subunit (By similarity). Component of the ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII), a multisubunit enzyme composed of 10 subunits. The complex is
CC composed of 3 respiratory subunits cytochrome b (MT-CYB), cytochrome c1
CC (CYC1-1 or CYC1-2) and Rieske protein (UCR1-1 or UCR1-2), 2 core
CC protein subunits MPPalpha1 (or MPPalpha2) and MPPB, and 5 low-molecular
CC weight protein subunits QCR7-1 (or QCR7-2), UCRQ-1 (or UCRQ-2), QCR9,
CC UCRY and probably QCR6-1 (or QCR6-2) (PubMed:18189341,
CC PubMed:18305213). The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI), resulting in different
CC assemblies (supercomplexes SCI(1)III(2) and SCI(2)III(4))
CC (PubMed:12970493). {ECO:0000250|UniProtKB:P11914,
CC ECO:0000269|PubMed:12970493, ECO:0000269|PubMed:18189341,
CC ECO:0000269|PubMed:18305213}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P11914}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18189341}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07257}; Matrix side
CC {ECO:0000250|UniProtKB:P07257}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZU25-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- CAUTION: Does not seem to have a protease activity as it lacks one of
CC the conserved zinc-binding sites. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE98617.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC006216; AAD12673.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32742.1; -; Genomic_DNA.
DR EMBL; AY065421; AAL38862.1; -; mRNA.
DR EMBL; AY091255; AAM14194.1; -; mRNA.
DR EMBL; AK226475; BAE98617.1; ALT_FRAME; mRNA.
DR EMBL; AY088384; AAM65922.1; -; mRNA.
DR PIR; D96559; D96559.
DR RefSeq; NP_175610.1; NM_104079.4. [Q9ZU25-1]
DR AlphaFoldDB; Q9ZU25; -.
DR SMR; Q9ZU25; -.
DR BioGRID; 26852; 7.
DR IntAct; Q9ZU25; 3.
DR MINT; Q9ZU25; -.
DR STRING; 3702.AT1G51980.1; -.
DR SwissPalm; Q9ZU25; -.
DR PaxDb; Q9ZU25; -.
DR PRIDE; Q9ZU25; -.
DR ProteomicsDB; 238903; -. [Q9ZU25-1]
DR EnsemblPlants; AT1G51980.1; AT1G51980.1; AT1G51980. [Q9ZU25-1]
DR GeneID; 841627; -.
DR Gramene; AT1G51980.1; AT1G51980.1; AT1G51980. [Q9ZU25-1]
DR KEGG; ath:AT1G51980; -.
DR Araport; AT1G51980; -.
DR TAIR; locus:2034096; AT1G51980.
DR eggNOG; KOG2067; Eukaryota.
DR InParanoid; Q9ZU25; -.
DR OMA; LKYHHSP; -.
DR PhylomeDB; Q9ZU25; -.
DR BioCyc; ARA:AT1G51980-MON; -.
DR BioCyc; MetaCyc:AT1G51980-MON; -.
DR PRO; PR:Q9ZU25; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZU25; baseline and differential.
DR Genevisible; Q9ZU25; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 60..503
FT /note="Probable mitochondrial-processing peptidase subunit
FT alpha-1, mitochondrial"
FT /id="PRO_0000026774"
FT CONFLICT 492
FT /note="V -> F (in Ref. 5; AAM65922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 54402 MW; 8BEB2853A07E924E CRC64;
MYRTAASRAR ALKGVLTRSL RPARYASSSA VAETSSSTPA YLSWLSGGSR AALTSLDMPL
QGVSLPPPLA DKVEPSKLQI TTLPNGLKIA SETTPNPAAS IGLYVDCGSI YEAPYFHGAT
HLLERMAFKS TLNRTHFRLV REIEAIGGNT SASASREQMS YTIDALKTYV PEMVEVLIDS
VRNPAFLDWE VNEELRKMKV EIAELAKNPM GFLLEAIHSA GYSGPLASPL YAPESALDRL
NGELLEEFMT ENFTAARMVL AASGVEHEEL LKVAEPLTSD LPNVPPQLAP KSQYVGGDFR
QHTGGEATHF AVAFEVPGWN NEKEAVTATV LQMLMGGGGS FSAGGPGKGM HSWLYRRVLN
EYQEVQSCTA FTSIFNDTGL FGIYGCSSPQ FAAKAIELAA KELKDVAGGK VNQAHLDRAK
AATKSAVLMN LESRMIAAED IGRQILTYGE RKPVDQFLKS VDQLTLKDIA DFTSKVISKP
LTMGSFGDVL AVPSYDTISS KFR
